Properties and Regulation of Aspartate Kinase from Barley Seedlings (Hordeum vulgare L.)
Open Access
- 1 January 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 59 (1) , 69-73
- https://doi.org/10.1104/pp.59.1.69
Abstract
Aspartate kinase (EC 2.7.2.4) has been purified 8-fold and characterized from germinating barley (Hordeum vulgare) seedlings. The enzyme is inhibited 50% by 0.7 mm l-lysine and almost completely at 5 mm. l-Methionine does not affect the enzyme on its own, but at low concentrations (0.1−1 mm) increases the inhibition in the presence of lysine, indicating that the two amino acids act as cooperative feedback regulators.This publication has 9 references indexed in Scilit:
- The use of amino acid analogues in biological studies.1976
- Changes in Enzyme Regulation during Growth of MaizePlant Physiology, 1975
- Aspartokinase from Wheat GermPlant Physiology, 1973
- Aspartokinase in Lemna minor LPlant Physiology, 1973
- Isolation and characterization of a lysine-sensitive aspartokinase from a multicellular plantBiochemical and Biophysical Research Communications, 1970
- Direct and Indirect Transfer of ATP and ADP across the Chloroplast EnvelopeZeitschrift für Naturforschung B, 1970
- Studies on the catalytic and regulatory properties of homoserine dehydrogenase of Zea mays rootsBiochimica et Biophysica Acta (BBA) - Enzymology, 1969
- The intracellular distribution of free nucleotides in the tobacco leaf. Formation of adenosine 5′-phosphate from adenosine 5′-triphosphate in the chloroplastsBiochemical Journal, 1968
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951